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P15692 (VEGFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 190. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vascular endothelial growth factor A

Short name=VEGF-A
Alternative name(s):
Vascular permeability factor
Short name=VPF
Gene names
Name:VEGFA
Synonyms:VEGF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length232 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth. Ref.27 Ref.30 Ref.33

Subunit structure

Homodimer; disulfide-linked. Also found as heterodimer with PGF By similarity.

Subcellular location

Secreted. Note: VEGF121 is acidic and freely secreted. VEGF165 is more basic, has heparin-binding properties and, although a signicant proportion remains cell-associated, most is freely secreted. VEGF189 is very basic, it is cell-associated after secretion and is bound avidly by heparin and the extracellular matrix, although it may be released as a soluble form by heparin, heparinase or plasmin. Ref.26 Ref.28 Ref.32

Tissue specificity

Isoform VEGF189, isoform VEGF165 and isoform VEGF121 are widely expressed. Isoform VEGF206 and isoform VEGF145 are not widely expressed.

Induction

Regulated by growth factors, cytokines, gonadotropins, nitric oxide, hypoxia, hypoglycemia and oncogenic mutations.

Involvement in disease

Microvascular complications of diabetes 1 (MVCD1) [MIM:603933]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Sequence similarities

Belongs to the PDGF/VEGF growth factor family.

Sequence caution

The sequence AAC63102.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAC63143.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence CAC19512.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

The sequence CAC19516.2 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.

Ontologies

Keywords
   Biological processAngiogenesis
Differentiation
   Cellular componentSecreted
   Coding sequence diversityAlternative initiation
Alternative promoter usage
Alternative splicing
   DomainSignal
   LigandHeparin-binding
   Molecular functionDevelopmental protein
Growth factor
Mitogen
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processVEGF-activated neuropilin signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

activation of protein kinase activity

Inferred from direct assay PubMed 18059339PubMed 20497126. Source: BHF-UCL

angiogenesis

Inferred from direct assay Ref.27. Source: UniProtKB

artery morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

basophil chemotaxis

Inferred from direct assay PubMed 17082651. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

branching morphogenesis of an epithelial tube

Inferred from sequence or structural similarity. Source: BHF-UCL

camera-type eye morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cardiac muscle fiber development

Inferred from sequence or structural similarity. Source: BHF-UCL

cardiac vascular smooth muscle cell development

Inferred from sequence or structural similarity. Source: BHF-UCL

cell maturation

Inferred from sequence or structural similarity. Source: BHF-UCL

cell migration involved in sprouting angiogenesis

Inferred from direct assay PubMed 18059339PubMed 20660291. Source: BHF-UCL

cellular response to hypoxia

Inferred from direct assay PubMed 10575000. Source: MGI

cellular response to vascular endothelial growth factor stimulus

Inferred from direct assay PubMed 18440775PubMed 20497126. Source: BHF-UCL

commissural neuron axon guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

coronary artery morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

coronary vein morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

dopaminergic neuron differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

endothelial cell chemotaxis

Inferred from direct assay PubMed 18440775. Source: BHF-UCL

epithelial cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

eye photoreceptor cell development

Inferred from sequence or structural similarity. Source: BHF-UCL

growth

Inferred from sequence or structural similarity. Source: BHF-UCL

heart morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

in utero embryonic development

Inferred from sequence or structural similarity. Source: BHF-UCL

induction of positive chemotaxis

Inferred from direct assay PubMed 19275959. Source: UniProtKB

kidney development

Inferred from sequence or structural similarity. Source: BHF-UCL

lactation

Inferred from sequence or structural similarity. Source: BHF-UCL

lung development

Inferred from sequence or structural similarity. Source: BHF-UCL

lymph vessel morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

macrophage differentiation

Inferred from direct assay PubMed 21149635. Source: DFLAT

mammary gland alveolus development

Inferred from sequence or structural similarity. Source: BHF-UCL

mesoderm development

Inferred from sequence or structural similarity. Source: BHF-UCL

monocyte differentiation

Inferred from direct assay PubMed 21149635. Source: DFLAT

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 10066377PubMed 11461089. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 18386220. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18093989. Source: BHF-UCL

nervous system development

Traceable author statement PubMed 15351965. Source: UniProtKB

outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

ovarian follicle development

Inferred from sequence or structural similarity. Source: BHF-UCL

patterning of blood vessels

Inferred from sequence or structural similarity. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive chemotaxis

Inferred from direct assay PubMed 20497126. Source: BHF-UCL

positive regulation of CREB transcription factor activity

Inferred from direct assay PubMed 20497126. Source: BHF-UCL

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 18440775. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from direct assay PubMed 19033661. Source: UniProtKB

positive regulation of axon extension involved in axon guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18440775PubMed 20497126PubMed 9202027. Source: BHF-UCL

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell adhesion

Inferred from direct assay PubMed 19674970. Source: UniProtKB

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell migration

Inferred from direct assay PubMed 17470632PubMed 7929439. Source: BHF-UCL

positive regulation of cell migration involved in sprouting angiogenesis

Inferred from direct assay PubMed 20551324. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 7929439. Source: BHF-UCL

positive regulation of cell proliferation by VEGF-activated platelet derived growth factor receptor signaling pathway

Inferred from direct assay PubMed 17470632PubMed 17470632PubMed 17470632. Source: BHF-UCL

positive regulation of cellular component movement

Inferred from direct assay PubMed 10527820PubMed 12744932. Source: BHF-UCL

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay PubMed 18440775PubMed 20497126PubMed 21245381. Source: BHF-UCL

positive regulation of endothelial cell migration

Inferred from direct assay PubMed 19033661. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay Ref.33PubMed 18386220. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of focal adhesion assembly

Inferred from direct assay Ref.33. Source: UniProtKB

positive regulation of gene expression

Inferred from direct assay PubMed 18386220. Source: UniProtKB

positive regulation of histone deacetylase activity

Inferred from direct assay PubMed 20497126. Source: BHF-UCL

positive regulation of intracellular signal transduction

Inferred from direct assay PubMed 20497126. Source: BHF-UCL

positive regulation of leukocyte migration

Traceable author statement PubMed 1312256. Source: BHF-UCL

positive regulation of mast cell chemotaxis

Inferred from direct assay PubMed 19275959. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of p38MAPK cascade

Inferred from direct assay PubMed 18386220. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18440775PubMed 20497126. Source: BHF-UCL

positive regulation of peptidyl-tyrosine autophosphorylation

Inferred from direct assay PubMed 20660291. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.33. Source: UniProtKB

positive regulation of positive chemotaxis

Inferred from direct assay PubMed 12744932PubMed 7929439. Source: BHF-UCL

positive regulation of protein autophosphorylation

Inferred from direct assay PubMed 20497126. Source: BHF-UCL

positive regulation of protein complex assembly

Inferred from direct assay Ref.33PubMed 19033661. Source: UniProtKB

positive regulation of protein kinase C signaling

Inferred from direct assay PubMed 18059339. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 18386220PubMed 19033661. Source: UniProtKB

positive regulation of receptor internalization

Inferred from direct assay PubMed 20660291. Source: BHF-UCL

positive regulation of retinal ganglion cell axon guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18059339PubMed 18093989. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter in response to hypoxia

Inferred from mutant phenotype PubMed 19652095. Source: BHF-UCL

positive regulation of vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay PubMed 1312256PubMed 7929439. Source: BHF-UCL

positive regulation of vascular permeability

Inferred from direct assay PubMed 16109918. Source: UniProtKB

post-embryonic camera-type eye development

Inferred from sequence or structural similarity. Source: BHF-UCL

primitive erythrocyte differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cell shape

Inferred from direct assay PubMed 10527820PubMed 7929439. Source: BHF-UCL

regulation of retinal ganglion cell axon guidance

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18093989. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from direct assay PubMed 16490744. Source: UniProtKB

surfactant homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

tube formation

Inferred from direct assay PubMed 19033661. Source: UniProtKB

vascular endothelial growth factor receptor signaling pathway

Inferred from direct assay PubMed 21245381. Source: BHF-UCL

vasculogenesis

Traceable author statement PubMed 15015550. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 17470632. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 17082651. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 16490744. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: InterPro

platelet alpha granule lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Non-traceable author statement PubMed 14570917. Source: UniProtKB

secretory granule

Inferred from direct assay PubMed 17082651. Source: UniProtKB

   Molecular_functionchemoattractant activity

Inferred from direct assay PubMed 17082651PubMed 19275959. Source: UniProtKB

cytokine activity

Inferred from direct assay PubMed 18440775. Source: BHF-UCL

extracellular matrix binding

Inferred by curator PubMed 14570917. Source: BHF-UCL

fibronectin binding

Inferred from direct assay PubMed 14570917. Source: BHF-UCL

growth factor activity

Inferred from direct assay PubMed 20497126PubMed 9202027. Source: BHF-UCL

heparin binding

Inferred from direct assay PubMed 15001987. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 12207021PubMed 1312256PubMed 22897854. Source: IntAct

platelet-derived growth factor receptor binding

Inferred from physical interaction PubMed 17470632. Source: BHF-UCL

protein heterodimerization activity

Inferred from direct assay PubMed 8702615. Source: MGI

protein homodimerization activity

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor agonist activity

Inferred from physical interaction PubMed 20660291. Source: BHF-UCL

vascular endothelial growth factor receptor 1 binding

Inferred from physical interaction PubMed 1312256. Source: BHF-UCL

vascular endothelial growth factor receptor 2 binding

Inferred from physical interaction PubMed 10022831PubMed 1417831PubMed 20660291. Source: BHF-UCL

vascular endothelial growth factor receptor binding

Inferred from physical interaction PubMed 10471394PubMed 11513746PubMed 9529250. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 17 isoforms produced by alternative promoter usage, alternative splicing and alternative initiation. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform VEGF206 (identifier: P15692-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform VEGF189 (identifier: P15692-2)

The sequence of this isoform differs from the canonical sequence as follows:
     166-182: Missing.
Isoform VEGF183 (identifier: P15692-3)

The sequence of this isoform differs from the canonical sequence as follows:
     160-182: Missing.
Isoform VEGF165 (identifier: P15692-4)

Also known as: VEGF;

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
Isoform VEGF148 (identifier: P15692-5)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     215-215: A → M
     216-232: Missing.
Isoform VEGF145 (identifier: P15692-6)

The sequence of this isoform differs from the canonical sequence as follows:
     166-226: Missing.
Isoform VEGF165B (identifier: P15692-8)

The sequence of this isoform differs from the canonical sequence as follows:
     141-141: K → N
     142-182: Missing.
     227-232: CDKPRR → SLTRKD
Isoform VEGF121 (identifier: P15692-9)

The sequence of this isoform differs from the canonical sequence as follows:
     142-226: Missing.
Note: No experimental confirmation available.
Isoform VEGF111 (identifier: P15692-10)

The sequence of this isoform differs from the canonical sequence as follows:
     132-226: Missing.
Note: No experimental confirmation available.
Isoform L-VEGF165 (identifier: P15692-11)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-141: K → N
     142-182: Missing.
Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).
Isoform L-VEGF121 (identifier: P15692-12)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     142-226: Missing.
Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).
Isoform L-VEGF189 (identifier: P15692-13)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     166-182: Missing.
Note: Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon. Post-translationally processed to produce the secreted VEGF peptide and a N-terminal peptide N-VEGF. The unprocessed protein and the N-VEGF peptide may localize to the nucleus (PubMed:15896327), the endoplasmic reticulum and the Golgi (PubMed:11731620) or the extracellular matrix (PubMed:11563986).
Isoform L-VEGF206 (identifier: P15692-14)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
Note: Gene prediction based on EST data. Produced by alternative promoter usage and alternative initiation. Starts at an alternative upstream CUG codon.
Isoform 15 (identifier: P15692-15)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     227-232: CDKPRR → SLTRKD
Note: Starts at an alternative upstream CUG codon.
Isoform 16 (identifier: P15692-16)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     160-182: Missing.
Note: Starts at an alternative upstream CUG codon.
Isoform 17 (identifier: P15692-17)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     141-182: KKSVRGKGKGQKRKRKKSRYKSWSVYVGARCCLMPWSLPGPH → N
     215-215: A → M
     216-232: Missing.
Note: Starts at an alternative upstream CUG codon.
Isoform 18 (identifier: P15692-18)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MTDRQTDTAP...AGPGRASETM
     132-226: Missing.
Note: Starts at an alternative upstream CUG codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.22 Ref.23 Ref.24
Chain27 – 232206Vascular endothelial growth factor A
PRO_0000023386

Amino acid modifications

Glycosylation1011N-linked (GlcNAc...)
Disulfide bond52 ↔ 94
Disulfide bond77Interchain
Disulfide bond83 ↔ 128
Disulfide bond86Interchain
Disulfide bond87 ↔ 130

Natural variations

Alternative sequence11M → MTDRQTDTAPSPSYHLLPGR RRTVDAAASRGQGPEPAPGG GVEGVGARGVALKLFVQLLG CSRFGGAVVRAGEAEPSGAA RSASSGREEPQPEEGEEEEE KEEERGPQWRLGARKPGSWT GEAAVCADSAPAARAPQALA RASGRGGRVARRGAEESGPP HSPSRRGSASRAGPGRASET M in isoform L-VEGF165, isoform L-VEGF121, isoform L-VEGF189, isoform L-VEGF206, isoform 15, isoform 16, isoform 17 and isoform 18.
VSP_038745
Alternative sequence132 – 22695Missing in isoform VEGF111 and isoform 18.
VSP_026781
Alternative sequence141 – 18242KKSVR…LPGPH → N in isoform 15 and isoform 17.
VSP_054111
Alternative sequence1411K → N in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165.
VSP_004618
Alternative sequence142 – 22685Missing in isoform VEGF121 and isoform L-VEGF121.
VSP_004620
Alternative sequence142 – 18241Missing in isoform VEGF148, isoform VEGF165, isoform VEGF165B and isoform L-VEGF165.
VSP_004619
Alternative sequence160 – 18223Missing in isoform VEGF183 and isoform 16.
VSP_004621
Alternative sequence166 – 22661Missing in isoform VEGF145.
VSP_004623
Alternative sequence166 – 18217Missing in isoform VEGF189 and isoform L-VEGF189.
VSP_004622
Alternative sequence2151A → M in isoform VEGF148 and isoform 17.
VSP_004624
Alternative sequence216 – 23217Missing in isoform VEGF148 and isoform 17.
VSP_004625
Alternative sequence227 – 2326CDKPRR → SLTRKD in isoform VEGF165B and isoform 15.
VSP_014783

Experimental info

Sequence conflict871C → S in AAC63143. Ref.8
Sequence conflict2101D → H in AAC63143. Ref.8

Secondary structure

............................... 232
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform VEGF206 [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: FB49F364446F4D01

FASTA23227,042
        10         20         30         40         50         60 
MNFLLSWVHW SLALLLYLHH AKWSQAAPMA EGGGQNHHEV VKFMDVYQRS YCHPIETLVD 

        70         80         90        100        110        120 
IFQEYPDEIE YIFKPSCVPL MRCGGCCNDE GLECVPTEES NITMQIMRIK PHQGQHIGEM 

       130        140        150        160        170        180 
SFLQHNKCEC RPKKDRARQE KKSVRGKGKG QKRKRKKSRY KSWSVYVGAR CCLMPWSLPG 

       190        200        210        220        230 
PHPCGPCSER RKHLFVQDPQ TCKCSCKNTD SRCKARQLEL NERTCRCDKP RR 

« Hide

Isoform VEGF189 [UniParc].

Checksum: 7B9759AD5871FF33
Show »

FASTA21525,173
Isoform VEGF183 [UniParc].

Checksum: F01CCEACD945D6CA
Show »

FASTA20924,422
Isoform VEGF165 (VEGF) [UniParc].

Checksum: CCE57097DD3779BD
Show »

FASTA19122,314
Isoform VEGF148 [UniParc].

Checksum: AE88400CA7757644
Show »

FASTA17420,218
Isoform VEGF145 [UniParc].

Checksum: D02ECA735FF6E9F8
Show »

FASTA17120,064
Isoform VEGF165B [UniParc].

Checksum: D25243E540AC79BD
Show »

FASTA19122,259
Isoform VEGF121 [UniParc].

Checksum: DDF4D6994249BED6
Show »

FASTA14717,219
Isoform VEGF111 [UniParc].

Checksum: 196B2BB49381BE87
Show »

FASTA13715,981
Isoform L-VEGF165 [UniParc].

Checksum: 053E9CA56725C07B
Show »

FASTA37140,738
Isoform L-VEGF121 [UniParc].

Checksum: 8D6F969601B2A9EF
Show »

FASTA32735,643
Isoform L-VEGF189 [UniParc].

Checksum: 8ADF6524B1835A2D
Show »

FASTA39543,597
Isoform L-VEGF206 [UniParc].

Checksum: AC807D3F21528D35
Show »

FASTA41245,467
Isoform 15 [UniParc].

Checksum: 1B89AFD7FABEC07B
Show »

FASTA37140,683
Isoform 16 [UniParc].

Checksum: 950279CF7A273A0E
Show »

FASTA38942,846
Isoform 17 [UniParc].

Checksum: 0152409399BAB1EB
Show »

FASTA35438,642
Isoform 18 [UniParc].

Checksum: FDF27C1251E3B613
Show »

FASTA31734,406

References

« Hide 'large scale' references
[1]"Vascular endothelial growth factor is a secreted angiogenic mitogen."
Leung D.W., Cachianes G., Kuang W.-J., Goeddel D.V., Ferrara N.
Science 246:1306-1309(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS VEGF189 AND VEGF165).
[2]"Vascular permeability factor, an endothelial cell mitogen related to PDGF."
Keck P.J., Hauser S.D., Krivi G., Sanzo K., Warren T., Feder J., Connolly D.T.
Science 246:1309-1312(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF189), PARTIAL PROTEIN SEQUENCE.
[3]"The human gene for vascular endothelial growth factor. Multiple protein forms are encoded through alternative exon splicing."
Tischer E., Mitchell R., Hartman T., Silva M., Gospodarowicz D., Fiddes J.C., Abraham J.A.
J. Biol. Chem. 266:11947-11954(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM VEGF189).
[4]"The vascular endothelial growth factor family: identification of a fourth molecular species and characterization of alternative splicing of RNA."
Houck K.A., Ferrara N., Winer J., Cachianes G., Li B., Leung D.W.
Mol. Endocrinol. 5:1806-1814(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM VEGF206).
[5]"AIDS-associated Kaposi's sarcoma cells in culture express vascular endothelial growth factor."
Weindel K., Marme D., Weich H.A.
Biochem. Biophys. Res. Commun. 183:1167-1174(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[6]"VEGF145, a secreted vascular endothelial growth factor isoform that binds to extracellular matrix."
Poltorak Z., Cohen T., Sivan R., Kandelis Y., Spira G., Vlodavsky I., Keshet E., Neufeld G.
J. Biol. Chem. 272:7151-7158(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF145).
[7]"Identification and characterization of a new splicing variant of vascular endothelial growth factor: VEGF183."
Lei J., Jiang A., Pei D.
Biochim. Biophys. Acta 1443:400-406(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF183).
Tissue: Kidney.
[8]"Identification of a human VPF/VEGF 3' untranslated region mediating hypoxia-induced mRNA stability."
Claffey K.P., Shih S.-C., Mullen A., Dziennis S., Cusick J.L., Abrams K.R., Lee S.W., Detmar M.
Mol. Biol. Cell 9:469-481(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-VEGF165).
Tissue: Mammary gland.
[9]"Heterogeneous vascular endothelial growth factor (VEGF) isoform mRNA and receptor mRNA expression in human glomeruli, and the identification of VEGF148 mRNA, a novel truncated splice variant."
Whittle C.J., Gillespie K.M., Harrison R., Mathieson P.W., Harper S.J.
Clin. Sci. 97:303-312(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF148).
Tissue: Renal glomerulus.
[10]"VEGF165b, an inhibitory splice variant of vascular endothelial growth factor, is down-regulated in renal cell carcinoma."
Bates D.O., Cui T.-G., Doughty J.M., Winkler M., Sugiono M., Shields J.D., Peat D., Gillatt D., Harper S.J.
Cancer Res. 62:4123-4131(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165B).
Tissue: Kidney.
[11]"Human cDNA for the vascular endothelial growth factor isoform VEGF165."
Murata H., Fukushima J., Hattori S., Okuda K., Yanagi H.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
Tissue: Hemangioendothelioma.
[12]"Human cDNA for vascular endothelial growth factor isoform VEGF121."
Sato J.D., Whitney R.G.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF121).
[13]"Cloning of vascular endothelial growth factor (VEGF) cDNA."
Liu J., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[14]"Cloning and identification of vascular endothelial growth factor isoform VEGF165."
Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Zheng M., Tan H.H., Lin S.G.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
Tissue: Heart.
[15]"Cloning and characterization of VEGF from LNCaP cells, a line of prostate cancer cells."
Koul S., Johnson T., Meacham R.B., Koul H.K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF165).
[16]"VEGF111, a new VEGF-A variant lacking exons 5, 6 and 7."
Mineur P.J., Colige A.C., Lambert C.A.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM VEGF111).
[17]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM VEGF165).
[18]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[19]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[20]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM L-VEGF121).
Tissue: Lung.
[21]SeattleSNPs variation discovery resource
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-232.
[22]"Synthesis and assembly of functionally active human vascular endothelial growth factor homodimers in insect cells."
Fiebich B.L., Jaeger B., Schoellmann C., Weindel K., Wilting J., Kochs G., Marme D., Hug H., Weich H.A.
Eur. J. Biochem. 211:19-26(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41.
[23]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41.
[24]"Human vascular permeability factor. Isolation from U937 cells."
Connolly D.T., Olander J.V., Heuvelman D., Nelson R., Monsell R., Siegel N., Haymore B.L., Leimgruber R., Feder J.
J. Biol. Chem. 264:20017-20024(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 27-36; 43-50 AND 59-81.
[25]"Human Muller cells express VEGF183, a novel spliced variant of vascular endothelial growth factor."
Jingjing L., Xue Y., Agarwal N., Roque R.S.
Invest. Ophthalmol. Vis. Sci. 40:752-759(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 114-209 (ISOFORM VEGF183).
Tissue: Retina.
[26]"A precursor form of vascular endothelial growth factor arises by initiation from an upstream in-frame CUG codon."
Tee M.K., Jaffe R.B.
Biochem. J. 359:219-226(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
[27]"Vascular endothelial growth factor induces cyclooxygenase-dependent proliferation of endothelial cells via the VEGF-2 receptor."
Murphy J.F., Fitzgerald D.J.
FASEB J. 15:1667-1669(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[28]"New vascular endothelial growth factor isoform generated by internal ribosome entry site-driven CUG translation initiation."
Huez I., Bornes S., Bresson D., Creancier L., Prats H.
Mol. Endocrinol. 15:2197-2210(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM L-VEGF189), PROCESSING, SUBCELLULAR LOCATION.
[29]"A common polymorphism in the 5'-untranslated region of the VEGF gene is associated with diabetic retinopathy in type 2 diabetes."
Awata T., Inoue K., Kurihara S., Ohkubo T., Watanabe M., Inukai K., Inoue I., Katayama S.
Diabetes 51:1635-1639(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MICROVASCULAR COMPLICATIONS OF DIABETES.
[30]"VEGF165b, an inhibitory vascular endothelial growth factor splice variant: mechanism of action, in vivo effect on angiogenesis and endogenous protein expression."
Woolard J., Wang W.-Y., Bevan H.S., Qiu Y., Morbidelli L., Pritchard-Jones R.O., Cui T.-G., Sugiono M., Waine E., Perrin R., Foster R., Digby-Bell J., Shields J.D., Whittles C.E., Mushens R.E., Gillatt D.A., Ziche M., Harper S.J., Bates D.O.
Cancer Res. 64:7822-7835(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM VEGF165B).
[31]"Control of the vascular endothelial growth factor internal ribosome entry site (IRES) activity and translation initiation by alternatively spliced coding sequences."
Bornes S., Boulard M., Hieblot C., Zanibellato C., Iacovoni J.S., Prats H., Touriol C.
J. Biol. Chem. 279:18717-18726(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121; L-VEGF165 AND L-VEGF189).
[32]"Nuclear localization of long-VEGF is associated with hypoxia and tumor angiogenesis."
Rosenbaum-Dekel Y., Fuchs A., Yakirevich E., Azriel A., Mazareb S., Resnick M.B., Levi B.Z.
Biochem. Biophys. Res. Commun. 332:271-278(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS L-VEGF121 AND L-VEGF165), PROCESSING, SUBCELLULAR LOCATION.
[33]"Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein."
Dixelius J., Olsson A.K., Thulin A., Lee C., Johansson I., Claesson-Welsh L.
Cancer Res. 66:2089-2097(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[34]"Vascular endothelial growth factor: crystal structure and functional mapping of the kinase domain receptor binding site."
Muller Y.A., Li B., Christinger H.W., Wells J.A., Cunningham B.C., de Vos A.M.
Proc. Natl. Acad. Sci. U.S.A. 94:7192-7197(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 34-135.
[35]"1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor."
Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
Protein Sci. 6:2250-2260(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 34-135.
[36]"The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93-A resolution: multiple copy flexibility and receptor binding."
Muller Y.A., Christinger H.W., Keyt B.A., de Vos A.M.
Structure 5:1325-1338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 34-135.
[37]"Crystal structure of the complex between VEGF and a receptor-blocking peptide."
Wiesmann C., Christinger H.W., Cochran A.G., Cunningham B.C., Fairbrother W.J., Keenan C.J., Meng G., de Vos A.M.
Biochemistry 37:17765-17772(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 39-134.
[38]"Solution structure of the heparin-binding domain of vascular endothelial growth factor."
Fairbrother W.J., Champe M.A., Christinger H.W., Keyt B.A., Starovasnik M.A.
Structure 6:637-648(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 137-215.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M32977 mRNA. Translation: AAA35789.1.
M27281 mRNA. Translation: AAA36807.1.
M63978 expand/collapse EMBL AC list , M63971, M63972, M63973, M63974, M63975, M63976, M63977 Genomic DNA. Translation: AAA36804.1.
S85192 mRNA. Translation: AAC63102.1. Different initiation.
AH006909 Genomic DNA. Translation: AAC63101.1.
X62568 mRNA. Translation: CAA44447.1.
AJ010438 mRNA. Translation: CAA09179.1.
AF022375 mRNA. Translation: AAC63143.1. Sequence problems.
AF091352 mRNA. Translation: AAD55345.1.
AF430806 mRNA. Translation: AAL27435.1.
AB021221 mRNA. Translation: BAA78418.1.
AF214570 mRNA. Translation: AAF19659.1.
AY047581 mRNA. Translation: AAK95847.1.
AF486837 mRNA. Translation: AAM03108.1.
AY766116 mRNA. Translation: AAV34601.1.
DQ229900 mRNA. Translation: ABB58912.1.
AB451322 mRNA. Translation: BAG70136.1.
AB451451 mRNA. Translation: BAG70265.1.
AL136131 Genomic DNA. Translation: CAC19512.2. Sequence problems.
AL136131 Genomic DNA. Translation: CAC19513.2.
AL136131 Genomic DNA. Translation: CAC19515.2.
AL136131 Genomic DNA. Translation: CAC19516.2. Sequence problems.
CH471081 Genomic DNA. Translation: EAX04229.1.
BC065522 mRNA. Translation: AAH65522.2.
AF437895 Genomic DNA. Translation: AAL27630.1.
AF062645 mRNA. Translation: AAC16730.1.
PIRA41551.
RefSeqNP_001020537.2. NM_001025366.2.
NP_001020538.2. NM_001025367.2.
NP_001020539.2. NM_001025368.2.
NP_001020540.2. NM_001025369.2.
NP_001020541.2. NM_001025370.2.
NP_001028928.1. NM_001033756.2.
NP_001165093.1. NM_001171622.1.
NP_001165094.1. NM_001171623.1.
NP_001165095.1. NM_001171624.1.
NP_001165096.1. NM_001171625.1.
NP_001165097.1. NM_001171626.1.
NP_001165098.1. NM_001171627.1.
NP_001165099.1. NM_001171628.1.
NP_001165100.1. NM_001171629.1.
NP_001165101.1. NM_001171630.1.
NP_001191313.1. NM_001204384.1.
NP_001191314.1. NM_001204385.1.
NP_001273973.1. NM_001287044.1.
NP_003367.4. NM_003376.5.
UniGeneHs.73793.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BJ1X-ray2.40V/W34-135[»]
1CZ8X-ray2.40V/W40-133[»]
1FLTX-ray1.70V/W38-135[»]
1KATNMR-V/W37-135[»]
1KMXNMR-A183-232[»]
1MJVX-ray2.10A/B40-134[»]
1MKGX-ray2.50A/B/C/D40-134[»]
1MKKX-ray1.32A/B40-134[»]
1QTYX-ray2.70R/S/V/W34-135[»]
1TZHX-ray2.60V/W34-135[»]
1TZIX-ray2.80V34-135[»]
1VGHNMR-A183-232[»]
1VPFX-ray2.50A/B/C/D34-135[»]
1VPPX-ray1.90V/W34-135[»]
2FJGX-ray2.80V/W34-135[»]
2FJHX-ray3.10V/W34-135[»]
2QR0X-ray3.50C/D/I/J/O/P/U/V39-135[»]
2VGHNMR-A183-232[»]
2VPFX-ray1.93A/B/C/D/E/F/G/H34-135[»]
3BDYX-ray2.60V34-135[»]
3P9WX-ray2.41A/C/E/G35-138[»]
3QTKX-ray1.85A/B/C/D/E/F34-135[»]
3S1BX-ray2.90V38-133[»]
3S1KX-ray2.55V/W34-135[»]
3V2AX-ray3.20A27-140[»]
4DEQX-ray2.65A/B183-232[»]
4GLNX-ray1.60E/F34-135[»]
4GLSX-ray1.60E/F34-135[»]
ProteinModelPortalP15692.
SMRP15692. Positions 39-133, 183-232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113265. 25 interactions.
DIPDIP-165N.
DIP-5740N.
DIP-5742N.
IntActP15692. 14 interactions.
MINTMINT-2834049.

Chemistry

BindingDBP15692.
ChEMBLCHEMBL1783.
DrugBankDB01076. Atorvastatin.
DB00112. Bevacizumab.
DB01136. Carvedilol.
DB01381. Ginkgo biloba.
DB01120. Gliclazide.
DB01017. Minocycline.
DB01270. Ranibizumab.
DB00641. Simvastatin.
GuidetoPHARMACOLOGY2644.

PTM databases

PhosphoSiteP15692.

Polymorphism databases

DMDM17380528.

Proteomic databases

PaxDbP15692.
PRIDEP15692.

Protocols and materials databases

DNASU7422.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324450; ENSP00000317598; ENSG00000112715.
ENST00000372064; ENSP00000361134; ENSG00000112715.
ENST00000372077; ENSP00000361148; ENSG00000112715. [P15692-9]
ENST00000413642; ENSP00000389864; ENSG00000112715.
ENST00000417285; ENSP00000388663; ENSG00000112715.
ENST00000425836; ENSP00000388465; ENSG00000112715.
ENST00000457104; ENSP00000409911; ENSG00000112715. [P15692-10]
ENST00000482630; ENSP00000421561; ENSG00000112715.
ENST00000518689; ENSP00000430829; ENSG00000112715. [P15692-3]
ENST00000518824; ENSP00000430002; ENSG00000112715. [P15692-8]
ENST00000520948; ENSP00000428321; ENSG00000112715. [P15692-2]
ENST00000523125; ENSP00000429008; ENSG00000112715. [P15692-5]
ENST00000523873; ENSP00000430479; ENSG00000112715. [P15692-1]
ENST00000523950; ENSP00000429643; ENSG00000112715. [P15692-4]
GeneID7422.
KEGGhsa:7422.
UCSCuc003owd.3. human. [P15692-5]
uc003owe.3. human. [P15692-4]
uc003owf.3. human. [P15692-13]
uc003owg.3. human. [P15692-3]
uc003owh.3. human. [P15692-1]
uc003owi.3. human. [P15692-8]
uc003owj.3. human. [P15692-9]
uc010jyx.3. human. [P15692-10]

Organism-specific databases

CTD7422.
GeneCardsGC06P043737.
HGNCHGNC:12680. VEGFA.
HPACAB005429.
MIM192240. gene.
603933. phenotype.
neXtProtNX_P15692.
PharmGKBPA37302.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG73329.
HOVERGENHBG000105.
InParanoidP15692.
KOK05448.
PhylomeDBP15692.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP15692.
BgeeP15692.
GenevestigatorP15692.

Family and domain databases

Gene3D2.10.160.10. 1 hit.
InterProIPR023581. PD_growth_factor_CS.
IPR000072. PDGF/VEGF_dom.
IPR027928. VEGF_C.
[Graphical view]
PfamPF00341. PDGF. 1 hit.
PF14554. VEGF_C. 1 hit.
[Graphical view]
SMARTSM00141. PDGF. 1 hit.
[Graphical view]
SUPFAMSSF57593. SSF57593. 1 hit.
PROSITEPS00249. PDGF_1. 1 hit.
PS50278. PDGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVEGFA. human.
EvolutionaryTraceP15692.
GeneWikiVascular_endothelial_growth_factor_A.
GenomeRNAi7422.
NextBio29060.
PROP15692.
SOURCESearch...

Entry information

Entry nameVEGFA_HUMAN
AccessionPrimary (citable) accession number: P15692
Secondary accession number(s): B5BU86 expand/collapse secondary AC list , H0Y2S8, H0Y407, H0Y414, H0Y462, H0Y8N2, H3BLW7, O60720, O75875, Q074Z4, Q16889, Q5UB46, Q6P0P5, Q96KJ0, Q96L82, Q96NW5, Q9H1W8, Q9H1W9, Q9UH58, Q9UL23
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 16, 2001
Last modified: April 16, 2014
This is version 190 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM